PSME2_MOUSE
ID PSME2_MOUSE Reviewed; 239 AA.
AC P97372; O35562;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Proteasome activator complex subunit 2;
DE AltName: Full=11S regulator complex subunit beta;
DE Short=REG-beta;
DE AltName: Full=Activator of multicatalytic protease subunit 2;
DE AltName: Full=Proteasome activator 28 subunit beta;
DE Short=PA28b;
DE Short=PA28beta;
GN Name=Psme2; Synonyms=Pa28b1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.BR;
RX PubMed=9162094; DOI=10.1007/s002510050246;
RA Jiang H., Monaco J.J.;
RT "Sequence and expression of mouse proteasome activator PA28 and the related
RT autoantigen Ki.";
RL Immunogenetics 46:93-98(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9590240;
RA Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y., Kasahara M.;
RT "Characterization of the mouse PA28 activator complex gene family: complete
RT organizations of the three member genes and a physical map of the
RT approximately 150-kb region containing the alpha- and beta-subunit genes.";
RL J. Immunol. 160:4923-4935(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=9914329; DOI=10.1007/s002510050476;
RA Li Y., Chambers J., Pang J., Ngo K., Peterson P.A., Leung W.P., Yang Y.;
RT "Characterization of the mouse proteasome regulator PA28b gene.";
RL Immunogenetics 49:149-157(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11345588; DOI=10.1007/s002510100308;
RA Yawata M., Murata S., Tanaka K., Ishigatsubo Y., Kasahara M.;
RT "Nucleotide sequence analysis of the ~35-kb segment containing interferon-
RT gamma-inducible mouse proteasome activator genes.";
RL Immunogenetics 53:119-129(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC efficient antigen processing. The PA28 activator complex enhances the
CC generation of class I binding peptides by altering the cleavage pattern
CC of the proteasome.
CC -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring.
CC -!- INDUCTION: By interferon gamma.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; U60329; AAC53296.1; -; mRNA.
DR EMBL; AB007138; BAA28837.1; -; Genomic_DNA.
DR EMBL; AF060195; AAC83999.1; -; Genomic_DNA.
DR EMBL; AB053120; BAB47405.1; -; Genomic_DNA.
DR EMBL; AK012344; BAB28175.1; -; mRNA.
DR EMBL; BC005680; AAH05680.1; -; mRNA.
DR EMBL; BC057859; AAH57859.1; -; mRNA.
DR CCDS; CCDS49494.1; -.
DR RefSeq; NP_001025026.1; NM_001029855.1.
DR RefSeq; NP_001268401.1; NM_001281472.1.
DR RefSeq; NP_035320.1; NM_011190.3.
DR PDB; 5MSK; X-ray; 3.60 A; A/B/C/D/E/F/G=1-239.
DR PDB; 5MX5; X-ray; 2.90 A; B/D/F/I/K/M=1-239.
DR PDBsum; 5MSK; -.
DR PDBsum; 5MX5; -.
DR AlphaFoldDB; P97372; -.
DR SMR; P97372; -.
DR BioGRID; 202433; 38.
DR BioGRID; 548745; 1.
DR IntAct; P97372; 3.
DR STRING; 10090.ENSMUSP00000100564; -.
DR iPTMnet; P97372; -.
DR PhosphoSitePlus; P97372; -.
DR SwissPalm; P97372; -.
DR CPTAC; non-CPTAC-3942; -.
DR EPD; P97372; -.
DR jPOST; P97372; -.
DR PaxDb; P97372; -.
DR PeptideAtlas; P97372; -.
DR PRIDE; P97372; -.
DR ProteomicsDB; 301991; -.
DR DNASU; 19188; -.
DR Ensembl; ENSMUST00000104958; ENSMUSP00000100564; ENSMUSG00000078153.
DR Ensembl; ENSMUST00000161807; ENSMUSP00000123798; ENSMUSG00000079197.
DR GeneID; 19188; -.
DR GeneID; 621823; -.
DR KEGG; mmu:19188; -.
DR KEGG; mmu:621823; -.
DR UCSC; uc007tzg.1; mouse.
DR CTD; 5721; -.
DR CTD; 621823; -.
DR MGI; MGI:1096365; Psme2.
DR VEuPathDB; HostDB:ENSMUSG00000078153; -.
DR VEuPathDB; HostDB:ENSMUSG00000079197; -.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR HOGENOM; CLU_062515_0_1_1; -.
DR InParanoid; P97372; -.
DR OMA; KKPPKCG; -.
DR OrthoDB; 1251022at2759; -.
DR PhylomeDB; P97372; -.
DR TreeFam; TF106236; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19188; 4 hits in 75 CRISPR screens.
DR BioGRID-ORCS; 621823; 1 hit in 53 CRISPR screens.
DR ChiTaRS; Psme2; mouse.
DR PRO; PR:P97372; -.
DR Proteomes; UP000000589; Chromosome 11.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97372; protein.
DR Bgee; ENSMUSG00000078153; Expressed in spleen and 53 other tissues.
DR ExpressionAtlas; P97372; baseline and differential.
DR Genevisible; P97372; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0061133; F:endopeptidase activator activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; IMP:MGI.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR003186; PA28_C.
DR InterPro; IPR036997; PA28_C_sf.
DR InterPro; IPR036996; PA28_N_sf.
DR InterPro; IPR009077; Proteasome_activ_PA28.
DR InterPro; IPR003185; Proteasome_activ_PA28_N.
DR InterPro; IPR036252; Proteasome_activ_sf.
DR PANTHER; PTHR10660; PTHR10660; 1.
DR Pfam; PF02251; PA28_alpha; 1.
DR Pfam; PF02252; PA28_beta; 1.
DR SUPFAM; SSF47216; SSF47216; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UL46"
FT CHAIN 2..239
FT /note="Proteasome activator complex subunit 2"
FT /id="PRO_0000161786"
FT REGION 65..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL46"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL46"
FT CONFLICT 152
FT /note="A -> P (in Ref. 2; AAC53296)"
FT /evidence="ECO:0000305"
FT HELIX 11..33
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:5MX5"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 98..128
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 138..180
FT /evidence="ECO:0007829|PDB:5MX5"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 186..222
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:5MX5"
SQ SEQUENCE 239 AA; 27057 MW; D8BB90F78CB0DD7C CRC64;
MAKPCGVRLS GEARKQVDVF RQNLFQEADD FLCTFLPRKI ISLSQLLQED SLNVADLSSL
RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGYLPGNEKL LALLALVKPE VWTLKEKCIL
VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK
DTHVMDYRAL VHERDEAAYG ALRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY
